1ai4 - Revision history

OCA at 06:30, 7 February 2024

OCA — Wed, 07 Feb 2024 06:30:43 GMT

←Older revision		Revision as of 06:30, 7 February 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ai4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AI4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ai4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AI4 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~, ~~<scene name='pdbligand=DHY:~~2~~-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.35Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https:~~/~~/en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase]~~, ~~with EC number [https~~:~~//www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=~~3~~.5.1.11 3.5.1.11]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHY:2-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [https://pdbe.org/1ai4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ai4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ai4 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [https://pdbe.org/1ai4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ai4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ai4 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/PAC_ECOLX PAC_ECOLX]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ai4 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ai4 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The enzyme penicillin acylase (penicillin amidohydrolase EC 3.5.1. 11) catalyses the cleavage of the amide bond in the benzylpenicillin (penicillin G) side-chain to produce phenylacetic acid and 6-aminopenicillanic acid (6-APA). The enzyme is of great pharmaceutical importance, as the product 6-APA is the starting point for the synthesis of many semi-synthetic penicillin antibiotics. Studies have shown that the enzyme is specific for hydrolysis of phenylacetamide derivatives, but is more tolerant of features in the rest of the substrate. It is this property that has led to many other applications for the enzyme, and greater knowledge of the enzyme's structure and specificity could facilitate engineering of the enzyme, enhancing its potential for chemical and industrial applications. An extensive study of the binding of a series of phenylacetic acid derivatives has been carried out. A measure of the relative degree of inhibition of the enzyme by each of the compounds has been obtained using a competitive inhibition assay, and the structures of a number of these complexes have been determined by X-ray crystallography. The structures reveal a clear rationale for the observed kinetic results, but show also that some of the ligands cause a conformational change within the binding pocket. This change can generally be understood in terms of the size and orientation of the ligand within the active site.The results reveal that ligand binding in penicillin acylase is facilitated by certain amino acid residues that can adopt two distinct, energetically favourable positions in order to accommodate a variety of compounds within the active site. The structures of these complexes provide evidence for conformational changes in the substrate-binding region that may act as a switch in the mechanism of autocatalytic processing of this enzyme.
-
-	Ligand-induced conformational change in penicillin acylase.,Done SH, Brannigan JA, Moody PC, Hubbard RE J Mol Biol. 1998 Nov 27;284(2):463-75. PMID:9813130<ref>PMID:9813130</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1ai4" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Penicillin acylase\|Penicillin acylase]]		*[[Penicillin acylase\|Penicillin acylase]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Penicillin amidase]]~~	+	[[Category: Done SH]]
-	[[Category: Done~~, S H]]~~	+
-	~~[[Category: Antibiotic resistance]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Ligand induced conformational change~~]]	+

OCA at 09:45, 26 May 2021

OCA — Wed, 26 May 2021 09:45:39 GMT

←Older revision		Revision as of 09:45, 26 May 2021
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	<StructureSection load='1ai4' size='340' side='right'caption='[[1ai4]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='1ai4' size='340' side='right'caption='[[1ai4]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ai4]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI4 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1AI4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ai4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AI4 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHY:2-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHY:2-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [~~http~~://pdbe.org/1ai4 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1ai4 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1ai4 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [https://pdbe.org/1ai4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ai4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ai4 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 07:33, 21 August 2019

OCA — Wed, 21 Aug 2019 07:33:04 GMT

←Older revision		Revision as of 07:33, 21 August 2019
Line 1:		Line 1:

	==PENICILLIN ACYLASE COMPLEXED WITH 3,4-DIHYDROXYPHENYLACETIC ACID==		==PENICILLIN ACYLASE COMPLEXED WITH 3,4-DIHYDROXYPHENYLACETIC ACID==
-	<StructureSection load='1ai4' size='340' side='right' caption='[[1ai4]], [[Resolution\|resolution]] 2.35Å' scene=''>	+	<StructureSection load='1ai4' size='340' side='right'caption='[[1ai4]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ai4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AI4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ai4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AI4 FirstGlance]. <br>
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ai/1ai4_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ai/1ai4_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 27:		Line 27:
	</div>		</div>
	<div class="pdbe-citations 1ai4" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ai4" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Penicillin acylase\|Penicillin acylase]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
		+	[[Category: Large Structures]]
	[[Category: Penicillin amidase]]		[[Category: Penicillin amidase]]
	[[Category: Done, S H]]		[[Category: Done, S H]]

OCA at 10:36, 15 November 2017

OCA — Wed, 15 Nov 2017 10:36:13 GMT

←Older revision		Revision as of 10:36, 15 November 2017
Line 1:		Line 1:
		+
	==PENICILLIN ACYLASE COMPLEXED WITH 3,4-DIHYDROXYPHENYLACETIC ACID==		==PENICILLIN ACYLASE COMPLEXED WITH 3,4-DIHYDROXYPHENYLACETIC ACID==
	<StructureSection load='1ai4' size='340' side='right' caption='[[1ai4]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='1ai4' size='340' side='right' caption='[[1ai4]], [[Resolution\|resolution]] 2.35Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHY:2-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHY:2-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [http://pdbe.org/1ai4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ai4 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [http://pdbe.org/1ai4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ai4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ai4 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	</div>		</div>
	<div class="pdbe-citations 1ai4" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ai4" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Penicillin acylase\|Penicillin acylase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:03, 9 February 2016

OCA — Tue, 09 Feb 2016 19:03:36 GMT

←Older revision		Revision as of 19:03, 9 February 2016
Line 15:		Line 15:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ai4 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 01:10, 11 September 2015

OCA — Fri, 11 Sep 2015 01:10:35 GMT

←Older revision		Revision as of 01:10, 11 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHY:2-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHY:2-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ai4 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [http://pdbe.org/1ai4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ai4 PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1ai4" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 11:52, 22 December 2014

OCA — Mon, 22 Dec 2014 11:52:56 GMT

←Older revision		Revision as of 11:52, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ai4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AI4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ai4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AI4 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHY:2-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHY:2-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ai4 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ai4 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Penicillin amidase]]		[[Category: Penicillin amidase]]
-	[[Category: Done, S H.]]	+	[[Category: Done, S H]]
	[[Category: Antibiotic resistance]]		[[Category: Antibiotic resistance]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Ligand induced conformational change]]		[[Category: Ligand induced conformational change]]

OCA at 09:36, 13 August 2014

OCA — Wed, 13 Aug 2014 09:36:59 GMT

←Older revision		Revision as of 09:36, 13 August 2014
Line 1:		Line 1:
-	[[~~Image~~:1ai4.~~png\|left~~\|200px]]	+	==PENICILLIN ACYLASE COMPLEXED WITH 3,4-DIHYDROXYPHENYLACETIC ACID==
		+	<StructureSection load='1ai4' size='340' side='right' caption='[[1ai4]], [[Resolution\|resolution]] 2.35Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1ai4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AI4 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHY:2-(3,4-DIHYDROXYPHENYL)ACETIC+ACID'>DHY</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ai4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ai4 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ai/1ai4_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The enzyme penicillin acylase (penicillin amidohydrolase EC 3.5.1. 11) catalyses the cleavage of the amide bond in the benzylpenicillin (penicillin G) side-chain to produce phenylacetic acid and 6-aminopenicillanic acid (6-APA). The enzyme is of great pharmaceutical importance, as the product 6-APA is the starting point for the synthesis of many semi-synthetic penicillin antibiotics. Studies have shown that the enzyme is specific for hydrolysis of phenylacetamide derivatives, but is more tolerant of features in the rest of the substrate. It is this property that has led to many other applications for the enzyme, and greater knowledge of the enzyme's structure and specificity could facilitate engineering of the enzyme, enhancing its potential for chemical and industrial applications. An extensive study of the binding of a series of phenylacetic acid derivatives has been carried out. A measure of the relative degree of inhibition of the enzyme by each of the compounds has been obtained using a competitive inhibition assay, and the structures of a number of these complexes have been determined by X-ray crystallography. The structures reveal a clear rationale for the observed kinetic results, but show also that some of the ligands cause a conformational change within the binding pocket. This change can generally be understood in terms of the size and orientation of the ligand within the active site.The results reveal that ligand binding in penicillin acylase is facilitated by certain amino acid residues that can adopt two distinct, energetically favourable positions in order to accommodate a variety of compounds within the active site. The structures of these complexes provide evidence for conformational changes in the substrate-binding region that may act as a switch in the mechanism of autocatalytic processing of this enzyme.

-	~~{{STRUCTURE_1ai4\| PDB=1ai4 \| SCENE= }}~~	+	Ligand-induced conformational change in penicillin acylase.,Done SH, Brannigan JA, Moody PC, Hubbard RE J Mol Biol. 1998 Nov 27;284(2):463-75. PMID:9813130<ref>PMID:9813130</ref>

-	~~===PENICILLIN ACYLASE COMPLEXED WITH 3~~,~~4-DIHYDROXYPHENYLACETIC ACID===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	==~~About this Structure~~==	+	*[[Penicillin acylase\|Penicillin acylase]]
-	[[~~1ai4~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI4 OCA].	+	== References ==
-		+	<references/>
-	==~~Reference~~==	+	__TOC__
-	<~~ref group="xtra">PMID:009813130<~~/~~ref~~><~~references group="xtra"~~/>	+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Penicillin amidase]]		[[Category: Penicillin amidase]]

OCA at 14:07, 8 November 2012

OCA — Thu, 08 Nov 2012 14:07:04 GMT

←Older revision		Revision as of 14:07, 8 November 2012
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	===PENICILLIN ACYLASE COMPLEXED WITH 3,4-DIHYDROXYPHENYLACETIC ACID===		===PENICILLIN ACYLASE COMPLEXED WITH 3,4-DIHYDROXYPHENYLACETIC ACID===

-	{{ABSTRACT_PUBMED_9813130}}

	==About this Structure==		==About this Structure==

OCA: Protected "1ai4" [edit=sysop:move=sysop]

OCA — Sun, 21 Oct 2012 14:26:59 GMT

Protected "1ai4" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:26, 21 October 2012